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Misfolding and aggregation of α-synuclein into toxic soluble oligomeric α-synuclein aggregates has been strongly correlated with the pathogenesis of Parkinson’s disease (PD). Here, we show that two different morphologically distinct

Misfolding and aggregation of α-synuclein into toxic soluble oligomeric α-synuclein aggregates has been strongly correlated with the pathogenesis of Parkinson’s disease (PD). Here, we show that two different morphologically distinct oligomeric α-synuclein aggregates are present in human post-mortem PD brain tissue and are responsible for the bulk of α-synuclein induced toxicity in brain homogenates from PD samples.

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    Date Created
    • 2015-07-22
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  • Text
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    Identifier
    • Digital object identifier: 10.3390/biom5031634
    • Identifier Type
      International standard serial number
      Identifier Value
      2218-273X

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    Xin, W., Emadi, S., Williams, S., Liu, Q., Schulz, P., He, P., . . . Sierks, M. (2015). Toxic Oligomeric Alpha-Synuclein Variants Present in Human Parkinson’s Disease Brains Are Differentially Generated in Mammalian Cell Models. Biomolecules, 5(3), 1634-1651. doi:10.3390/biom5031634

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